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Apolipoprotein M: Progress in understanding its regulation and metabolic functions

Christoffersen, C. ; Dahlbäck, Björn LU and Nielsen, L. B. (2006) In Scandinavian Journal of Clinical & Laboratory Investigation 66(7). p.631-637
Abstract
ApoM is a novel apolipoprotein mainly present in high-density lipoprotein (HDL). It belongs to the lipocalin protein superfamily and may bind a small but so far unknown lipophilic ligand. It is secreted without cleavage of its hydrophobic signal peptide, which probably anchors apoM in the phospholipid moiety of plasma lipoproteins. Recent studies suggest that apoM may affect HDL metabolism and have anti-atherogenic functions. The subfraction of human HDL that contains apoM therefore protects LDL from oxidation and mediates cholesterol efflux more efficiently then HDL without apoM. In addition to hepatocytes, apoM is highly expressed in kidney proximal tubule cells. Recent data suggest that apoM is secreted into the pre-urine from the... (More)
ApoM is a novel apolipoprotein mainly present in high-density lipoprotein (HDL). It belongs to the lipocalin protein superfamily and may bind a small but so far unknown lipophilic ligand. It is secreted without cleavage of its hydrophobic signal peptide, which probably anchors apoM in the phospholipid moiety of plasma lipoproteins. Recent studies suggest that apoM may affect HDL metabolism and have anti-atherogenic functions. The subfraction of human HDL that contains apoM therefore protects LDL from oxidation and mediates cholesterol efflux more efficiently then HDL without apoM. In addition to hepatocytes, apoM is highly expressed in kidney proximal tubule cells. Recent data suggest that apoM is secreted into the pre-urine from the tubule cells but is normally taken up again in a megalin-dependent fashion. Further studies of mice with genetically modified apoM expression will be essential to unravel the potential roles of apoM in lipoprotein metabolism, atherosclerosis and kidney biology. (Less)
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
megalin, HDL metabolism, cholesterol efflux, apoM, atherosclerosis, oxidation
in
Scandinavian Journal of Clinical & Laboratory Investigation
volume
66
issue
7
pages
631 - 637
publisher
Informa Healthcare
external identifiers
  • wos:000242102600011
  • scopus:33751073952
  • pmid:17101555
ISSN
1502-7686
DOI
10.1080/00365510600885500
language
English
LU publication?
yes
id
aa06e956-adb8-4650-a951-6657487d96de (old id 685423)
date added to LUP
2016-04-01 16:02:12
date last changed
2020-10-07 04:19:47
@article{aa06e956-adb8-4650-a951-6657487d96de,
  abstract     = {ApoM is a novel apolipoprotein mainly present in high-density lipoprotein (HDL). It belongs to the lipocalin protein superfamily and may bind a small but so far unknown lipophilic ligand. It is secreted without cleavage of its hydrophobic signal peptide, which probably anchors apoM in the phospholipid moiety of plasma lipoproteins. Recent studies suggest that apoM may affect HDL metabolism and have anti-atherogenic functions. The subfraction of human HDL that contains apoM therefore protects LDL from oxidation and mediates cholesterol efflux more efficiently then HDL without apoM. In addition to hepatocytes, apoM is highly expressed in kidney proximal tubule cells. Recent data suggest that apoM is secreted into the pre-urine from the tubule cells but is normally taken up again in a megalin-dependent fashion. Further studies of mice with genetically modified apoM expression will be essential to unravel the potential roles of apoM in lipoprotein metabolism, atherosclerosis and kidney biology.},
  author       = {Christoffersen, C. and Dahlbäck, Björn and Nielsen, L. B.},
  issn         = {1502-7686},
  language     = {eng},
  number       = {7},
  pages        = {631--637},
  publisher    = {Informa Healthcare},
  series       = {Scandinavian Journal of Clinical & Laboratory Investigation},
  title        = {Apolipoprotein M: Progress in understanding its regulation and metabolic functions},
  url          = {http://dx.doi.org/10.1080/00365510600885500},
  doi          = {10.1080/00365510600885500},
  volume       = {66},
  year         = {2006},
}